Primary structure of the plant serpin BSZ7 having the capacity of chymotrypsin inhibition

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Standard

Primary structure of the plant serpin BSZ7 having the capacity of chymotrypsin inhibition. / Rasmussen, Søren K.; Klausen, Janne; Hejgaard, Jørn; Svensson, Birte; Svendsen, Ib.

In: Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology, Vol. 1297, No. 2, 1996, p. 127-130.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Rasmussen, SK, Klausen, J, Hejgaard, J, Svensson, B & Svendsen, I 1996, 'Primary structure of the plant serpin BSZ7 having the capacity of chymotrypsin inhibition', Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology, vol. 1297, no. 2, pp. 127-130. https://doi.org/10.1016/S0167-4838(96)00115-X

APA

Rasmussen, S. K., Klausen, J., Hejgaard, J., Svensson, B., & Svendsen, I. (1996). Primary structure of the plant serpin BSZ7 having the capacity of chymotrypsin inhibition. Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology, 1297(2), 127-130. https://doi.org/10.1016/S0167-4838(96)00115-X

Vancouver

Rasmussen SK, Klausen J, Hejgaard J, Svensson B, Svendsen I. Primary structure of the plant serpin BSZ7 having the capacity of chymotrypsin inhibition. Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology. 1996;1297(2):127-130. https://doi.org/10.1016/S0167-4838(96)00115-X

Author

Rasmussen, Søren K. ; Klausen, Janne ; Hejgaard, Jørn ; Svensson, Birte ; Svendsen, Ib. / Primary structure of the plant serpin BSZ7 having the capacity of chymotrypsin inhibition. In: Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology. 1996 ; Vol. 1297, No. 2. pp. 127-130.

Bibtex

@article{9e7cc09a8d144b91925c83b473a3dfc2,
title = "Primary structure of the plant serpin BSZ7 having the capacity of chymotrypsin inhibition",
abstract = "The primary structure of barley grain serpin BSZ7 was deduced from a cDNA encoding 397 amino-acid residues, More than 70% of the residues were confirmed by sequencing peptide fragments. The N-terminus was identified as an acetylated Ala by using mass spectrometry coupled with amino-acid analysis. None of the four putative N-glycosylation sites were found to be glycosylated. The positional identity of BSZ7 with plant and mammalian serpins is 69-72% and 25-32%, respectively.",
keywords = "Acetylated N-terminus, Amino acid sequence, CDNA, Hordeum vulgare, Protein Z",
author = "Rasmussen, {S{\o}ren K.} and Janne Klausen and J{\o}rn Hejgaard and Birte Svensson and Ib Svendsen",
year = "1996",
doi = "10.1016/S0167-4838(96)00115-X",
language = "English",
volume = "1297",
pages = "127--130",
journal = "B B A - Proteins and Proteomics",
issn = "1570-9639",
publisher = "Elsevier",
number = "2",

}

RIS

TY - JOUR

T1 - Primary structure of the plant serpin BSZ7 having the capacity of chymotrypsin inhibition

AU - Rasmussen, Søren K.

AU - Klausen, Janne

AU - Hejgaard, Jørn

AU - Svensson, Birte

AU - Svendsen, Ib

PY - 1996

Y1 - 1996

N2 - The primary structure of barley grain serpin BSZ7 was deduced from a cDNA encoding 397 amino-acid residues, More than 70% of the residues were confirmed by sequencing peptide fragments. The N-terminus was identified as an acetylated Ala by using mass spectrometry coupled with amino-acid analysis. None of the four putative N-glycosylation sites were found to be glycosylated. The positional identity of BSZ7 with plant and mammalian serpins is 69-72% and 25-32%, respectively.

AB - The primary structure of barley grain serpin BSZ7 was deduced from a cDNA encoding 397 amino-acid residues, More than 70% of the residues were confirmed by sequencing peptide fragments. The N-terminus was identified as an acetylated Ala by using mass spectrometry coupled with amino-acid analysis. None of the four putative N-glycosylation sites were found to be glycosylated. The positional identity of BSZ7 with plant and mammalian serpins is 69-72% and 25-32%, respectively.

KW - Acetylated N-terminus

KW - Amino acid sequence

KW - CDNA

KW - Hordeum vulgare

KW - Protein Z

U2 - 10.1016/S0167-4838(96)00115-X

DO - 10.1016/S0167-4838(96)00115-X

M3 - Journal article

C2 - 8917613

AN - SCOPUS:0030591752

VL - 1297

SP - 127

EP - 130

JO - B B A - Proteins and Proteomics

JF - B B A - Proteins and Proteomics

SN - 1570-9639

IS - 2

ER -

ID: 204470420